FLVC1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: FLVC1_HUMAN
• UniProt AC: Q9Y5Y0
• Protein Name: Feline leukemia virus subgroup C receptor-related protein 1
• Gene Name: FLVCR1
• Organism: Homo sapiens (Human).
• Sequence Length: 555
• Subcellular Localization: Isoform 1: Cell membrane; Multi-pass membrane protein.; Isoform 2: Mitochondrion membrane; Multi-pass membrane protein.
• Protein Description: Isoform 1: Heme transporter that exports cytoplasmic heme. It can also export coproporphyrin and protoporphyrin IX, which are both intermediate products in the heme biosynthetic pathway. Does not export bilirubin. Heme export depends on the presence of HPX and is required to maintain intracellular free heme balance, protecting cells from heme toxicity. Heme export provides protection from heme or ferrous iron toxicities in liver, brain, sensory neurons and during erythtopoiesis, a process in which heme synthesis intensifies. Causes susceptibility to FeLV-C in vitro.; Isoform 2: Heme transporter that promotes heme efflux from the mitochondrion to the cytoplasm. Essential for erythroid differentiation..
• Protein Sequence: MARPDDEEGAAVAPGHPLAKGYLPLPRGAPVGKESVELQNGPKAGTFPVNGAPRDSLAAASGVLGGPQTPLAPEEETQARLLPAGAGAETPGAESSPLPLTALSPRRFVVLLIFSLYSLVNAFQWIQYSIISNVFEGFYGVTLLHIDWLSMVYMLAYVPLIFPATWLLDTRGLRLTALLGSGLNCLGAWIKCGSVQQHLFWVTMLGQCLCSVAQVFILGLPSRIASVWFGPKEVSTACATAVLGNQLGTAVGFLLPPVLVPNTQNDTNLLACNISTMFYGTSAVATLLFILTAIAFKEKPRYPPSQAQAALQDSPPEEYSYKKSIRNLFKNIPFVLLLITYGIMTGAFYSVSTLLNQMILTYYEGEEVNAGRIGLTLVVAGMVGSILCGLWLDYTKTYKQTTLIVYILSFIGMVIFTFTLDLRYIIIVFVTGGVLGFFMTGYLPLGFEFAVEITYPESEGTSSGLLNASAQIFGILFTLAQGKLTSDYGPKAGNIFLCVWMFIGIILTALIKSDLRRHNINIGITNVDVKAIPADSPTDQEPKTVMLSKQSESAI

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MARPDDEEG ------CCCCCCCCC	31.54	-
20	Ubiquitination	APGHPLAKGYLPLPR CCCCCCCCCCCCCCC	56.63	-
22	Phosphorylation	GHPLAKGYLPLPRGA CCCCCCCCCCCCCCC	12.39	25884760
33	Ubiquitination	PRGAPVGKESVELQN CCCCCCCCCCEECCC	47.23	21906983
43	Ubiquitination	VELQNGPKAGTFPVN EECCCCCCCCCCCCC	61.93	-
46	Phosphorylation	QNGPKAGTFPVNGAP CCCCCCCCCCCCCCC	29.62	28122231
56	Phosphorylation	VNGAPRDSLAAASGV CCCCCHHHHHHHHCC	22.61	30243723
61	Phosphorylation	RDSLAAASGVLGGPQ HHHHHHHHCCCCCCC	25.38	30243723
69	Phosphorylation	GVLGGPQTPLAPEEE CCCCCCCCCCCCHHH	24.33	30243723
90	Phosphorylation	PAGAGAETPGAESSP CCCCCCCCCCCCCCC	26.87	26657352
95	Phosphorylation	AETPGAESSPLPLTA CCCCCCCCCCCCCHH	36.40	27732954
96	Phosphorylation	ETPGAESSPLPLTAL CCCCCCCCCCCCHHC	23.20	27732954
101	Phosphorylation	ESSPLPLTALSPRRF CCCCCCCHHCCHHHH	24.50	27732954
104	Phosphorylation	PLPLTALSPRRFVVL CCCCHHCCHHHHHHH	17.56	24719451
265	N-linked_Glycosylation	VLVPNTQNDTNLLAC EECCCCCCCCCEEEE	56.91	UniProtKB CARBOHYD
273	N-linked_Glycosylation	DTNLLACNISTMFYG CCCEEEEEHHHHHHC	26.16	UniProtKB CARBOHYD
322	Ubiquitination	PPEEYSYKKSIRNLF CCHHHCHHHHHHHHH	33.82	21906983
323	Ubiquitination	PEEYSYKKSIRNLFK CHHHCHHHHHHHHHH	42.77	-
398	Phosphorylation	WLDYTKTYKQTTLIV HHCCCCCCCHHHHHH	11.58	22210691
401	Phosphorylation	YTKTYKQTTLIVYIL CCCCCCHHHHHHHHH	21.29	22210691
417	Phosphorylation	FIGMVIFTFTLDLRY HHHHHHHHHHCCCCC	12.46	22210691
419	Phosphorylation	GMVIFTFTLDLRYII HHHHHHHHCCCCCEE	19.12	22210691
530	Ubiquitination	GITNVDVKAIPADSP EEEEECEEECCCCCC	35.81	21906983
536	Phosphorylation	VKAIPADSPTDQEPK EEECCCCCCCCCCCC	31.63	30266825
538	Phosphorylation	AIPADSPTDQEPKTV ECCCCCCCCCCCCEE	55.02	30266825
543	Ubiquitination	SPTDQEPKTVMLSKQ CCCCCCCCEEEECCC	53.66	-
544	Phosphorylation	PTDQEPKTVMLSKQS CCCCCCCEEEECCCC	23.12	-
548	Phosphorylation	EPKTVMLSKQSESAI CCCEEEECCCCCCCC	15.56	-
549	Ubiquitination	PKTVMLSKQSESAI- CCEEEECCCCCCCC-	54.61	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of FLVC1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of FLVC1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of FLVC1_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of FLVC1_HUMAN !!

Drug and Disease Associations

• Kegg Disease
• H01036: Posterior column ataxia with retinitis pigmentosa (PCARP)
• OMIM Disease
• 609033: Posterior column ataxia with retinitis pigmentosa (PCARP)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Acetylation

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-536, AND MASS SPECTROMETRY.
PubMed: 19413330

Phosphorylation

"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, AND MASSSPECTROMETRY.
PubMed: 19690332

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-536, AND MASS SPECTROMETRY.
PubMed: 19413330